BMRB Entry 16675
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16675
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Title: The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum PubMed: 20195702
Deposition date: 2010-01-14 Original release date: 2010-05-05
Authors: Kumeta, Hiroyuki; Miwa, Noriko; Ogura, Kenji; Kai, Yuko; Mizukoshi, Toshimi; Shimba, Nobuhisa; Suzuki, Ei-ichiro; Inagaki, Fuyuhiko
Citation: Kumeta, Hiroyuki; Miwa, Noriko; Ogura, Kenji; Kai, Yuko; Mizukoshi, Toshimi; Shimba, Nobuhisa; Suzuki, Ei-ichiro; Inagaki, Fuyuhiko. "The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum." J. Biomol. NMR 46, 251-255 (2010).
Assembly members:
protein-glutaminase, polymer, 185 residues, 19875.396 Da.
Natural source: Common Name: Chryseobacterium proteolyticum Taxonomy ID: 118127 Superkingdom: Bacteria Kingdom: not available Genus/species: Chryseobacterium proteolyticum
Experimental source: Production method: recombinant technology Host organism: Corynebacterium glutamicum
Entity Sequences (FASTA):
protein-glutaminase: LASVIPDVATLNSLFNQIKN
QSCGTSTASSPCITFRYPVD
GCYARAHKMRQILMNNGYDC
EKQFVYGNLKASTGTCCVAW
SYHVAILVSYKNASGVTEKR
IIDPSLFSSGPVTDTAWRNA
CVNTSCGSASVSSYANTAGN
VYYRSPSNSYLYDNNLINTN
CVLTKFSLLSGCSPSPAPDV
SSCGF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 797 |
| 15N chemical shifts | 205 |
| 1H chemical shifts | 1247 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | protein-glutaminase | 1 |
Entities:
Entity 1, protein-glutaminase 185 residues - 19875.396 Da.
| 1 | LEU | ALA | SER | VAL | ILE | PRO | ASP | VAL | ALA | THR | ||||
| 2 | LEU | ASN | SER | LEU | PHE | ASN | GLN | ILE | LYS | ASN | ||||
| 3 | GLN | SER | CYS | GLY | THR | SER | THR | ALA | SER | SER | ||||
| 4 | PRO | CYS | ILE | THR | PHE | ARG | TYR | PRO | VAL | ASP | ||||
| 5 | GLY | CYS | TYR | ALA | ARG | ALA | HIS | LYS | MET | ARG | ||||
| 6 | GLN | ILE | LEU | MET | ASN | ASN | GLY | TYR | ASP | CYS | ||||
| 7 | GLU | LYS | GLN | PHE | VAL | TYR | GLY | ASN | LEU | LYS | ||||
| 8 | ALA | SER | THR | GLY | THR | CYS | CYS | VAL | ALA | TRP | ||||
| 9 | SER | TYR | HIS | VAL | ALA | ILE | LEU | VAL | SER | TYR | ||||
| 10 | LYS | ASN | ALA | SER | GLY | VAL | THR | GLU | LYS | ARG | ||||
| 11 | ILE | ILE | ASP | PRO | SER | LEU | PHE | SER | SER | GLY | ||||
| 12 | PRO | VAL | THR | ASP | THR | ALA | TRP | ARG | ASN | ALA | ||||
| 13 | CYS | VAL | ASN | THR | SER | CYS | GLY | SER | ALA | SER | ||||
| 14 | VAL | SER | SER | TYR | ALA | ASN | THR | ALA | GLY | ASN | ||||
| 15 | VAL | TYR | TYR | ARG | SER | PRO | SER | ASN | SER | TYR | ||||
| 16 | LEU | TYR | ASP | ASN | ASN | LEU | ILE | ASN | THR | ASN | ||||
| 17 | CYS | VAL | LEU | THR | LYS | PHE | SER | LEU | LEU | SER | ||||
| 18 | GLY | CYS | SER | PRO | SER | PRO | ALA | PRO | ASP | VAL | ||||
| 19 | SER | SER | CYS | GLY | PHE |
Samples:
CN-label: protein glutaminase, [U-13C; U-15N], 1.15 mM; D2O 5%; H2O 95%
sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | CN-label | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | CN-label | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | CN-label | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | CN-label | isotropic | sample_conditions_1 |
| 3D HNCO | CN-label | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | CN-label | isotropic | sample_conditions_1 |
| 3D HNCA | CN-label | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | CN-label | isotropic | sample_conditions_1 |
| 3D HN(CA)HA | CN-label | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | CN-label | isotropic | sample_conditions_1 |
| 3D HNCACB | CN-label | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | CN-label | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | CN-label | isotropic | sample_conditions_1 |
| 2D HbCbCgCdHd | CN-label | isotropic | sample_conditions_1 |
| 2D HbCbCgCdCeHe | CN-label | isotropic | sample_conditions_1 |
Software:
VNMR v6.1C, Varian - collection
NMRPipe v5.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.111, Goddard - chemical shift assignment, peak picking
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts